4 research outputs found
The effect of lithological diversity of feed on process efficiency indexes in KGHM Polska Mied藕 S.A. concentrator plants
W artykule przedstawiono efektywno艣膰 wzbogacania urobku dostarczonego z zak艂ad贸w g贸rniczych w 艣wietle jego w艂a艣ciwo艣ci fizykochemicznych, charakterystycznych dla trzech g艂贸wnych odmian litologicznych ska艂 z艂o偶owych b臋d膮cych jego sk艂adnikami. W tym celu okre艣lono podatno艣膰 na wzbogacanie poszczeg贸lnych wydziele艅 litologicznych obecnych w urobku, stanowi膮cym nadaw臋 do procesu wzbogacania. Na przyk艂adzie jednego z Rejon贸w O/ZWR wyznaczono zale偶no艣膰 funkcyjn膮 pomi臋dzy uzyskiem a jako艣ci膮 koncentratu [蔚 = f(尾)], kt贸ra obrazuje wp艂yw zawarto艣ci sk艂adnik贸w litologicznych na osi膮gane wska藕niki wzbogacania. Wykazano, 偶e przemys艂owe wzbogacanie jest bardzo czu艂e na zmiany jako艣ci nadawy w aspekcie zawarto艣ci poszczeg贸lnych sk艂adnik贸w litologicznych, a tak偶e udzia艂u g艂贸wnych sk艂adnik贸w u偶ytecznych i towarzysz膮cych.The paper presents the performance of ore beneficiation process carried out on KGHM Polska Mied藕 S.A. run-of-mine ore relating to its physicochemical properties. The properties are strongly associated with the lithology of rock formations. The susceptibility of specific lithological fraction occurred in the ore for the beneficiation process is described. Functional relationship between recovery and concentrate grade [蔚 = f(尾)] was developed as the example for one of the KGHM Polska Mied藕 S.A. concentrators plants. The variety of ore properties and its effect on process efficiency is discussed. It has been proved that industrial process efficiency is very sensitive to both the alteration of lithological fractions and the content of major valuable metals and accompanying compounds
Structure of the Intrinsically Disordered Protein Otholith in Solution at Different Protein and Salt Concentrations
Two members of the intrinsically disordered proteins (IDP) family (OMM-64 and STM) have been studied by means of small angle neutron scattering (SANS), dynamic light scattering (DLS) and fluorescence correlation spectroscopy (FCS). SANS curves of the proteins in D2O buffers have been measured for a range of Na+ and Ca2+ salts concentrations. The same samples have been measured using DLS in order to estimate their apparent hydrodynamic radii (Rh) and the scattering intensity in the q = 0 limit. The size of the proteins as a function of Na+ and Ca2+ concentrations had been measured in nano-molar concentrations using FCS. Fits to the SANS data suggest a coiled structure of the proteins in solution. For the first time SANS curves of proteins embedded in calcium carbonate crystals have been measured. Also a coiled structure has been found (slope = -2). Exact values of the radius of gyration (Rg) from SANS need measurements at smaller q-values